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Protein–protein associations are fundamental to biological mechanisms, creating a need for a book that covers the basic principles of protein–protein association. This book has been developed from lectures given to graduate students in cell and molecular biology. The general principles are accompanied by guided reading of informative classic papers. This book should be useful for faculties organizing similar classes, and also for students and researchers who wish to learn on their own. Part of the Biophysical Society series.

Copyright © IOP Publishing Ltd 2019
Online ISBN: 978-0-7503-2412-0 • Print ISBN: 978-0-7503-2410-6

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Front matter

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Pages 1-1 to 1-17
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Size and shape of protein molecules at the nm level determined by sedimentation, gel filtration and electron microscopy

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Pages 2-1 to 2-7

Basic thermodynamics of reversible association

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Pages 3-1 to 3-9

The nature of the protein–protein bond, à la Chothia and Janin

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Pages 4-1 to 4-4

The structure of an antibody bound to its protein ligand—lock and key versus induced fit and conformational selection

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Pages 5-1 to 5-5

The complex of growth hormone with its receptor—one protein interface binds two partners

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Pages 6-1 to 6-7

The hot spot in protein–protein interfaces

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Pages 7-1 to 7-7

Cooperativity in protein–protein association and efficiency of bonds

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Pages 8-1 to 8-5

Kinetics of protein–protein association and dissociation

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Pages 9-1 to 9-8

Techniques for measuring protein–protein association—use and misuse of ELISA

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Pages 10-1 to 10-8

Fibronectin, the FNIII domain, and artificial antibodies

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Pages 11-1 to 11-5

Association of intrinsically disordered proteins—flexible binding partners

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